Digestion of asparagine-linked oligosaccharides by endo-beta-N-acetylglucosaminidase in the human skin fibroblasts obtained from fucosidosis patients.
The substrate specificity of human endo-beta-N-acetylglucosaminidase was studied by using the homogenate of cultured skin fibroblasts of fucosidosis patients as an enzyme source. The results indicate that biantennary complex type asparagine-linked sugar chains as well as high mannose type sugar chains are cleaved by the enzyme action. None of the sugar chains with a fucosyl residue on the proximal N-acetylglucosamine of their N,N'-diacetylchitobiose moieties was cleaved. These results proved enzymatically the mechanism of production of oligosaccharides detected in the urine of various exoglycosidase deficiencies.
D000118:Acetylglucosaminidase / Q000502:physiology*; D001216:Asparagine / Q000378:metabolism*; D002239:Carbohydrate Metabolism, Inborn Errors / Q000201:enzymology*; D005347:Fibroblasts / Q000201:enzymology; D005643:Fucose / Q000378:metabolism*; D006596:Hexosaminidases / Q000502:physiology*; D006801:Humans; D006868:Hydrolysis; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D009844:Oligosaccharides / Q000378:metabolism*; D012867:Skin / Q000201:enzymology*; D013379:Substrate Specificity
D009844:Oligosaccharides; D005643:Fucose; D001216:Asparagine; D006596:Hexosaminidases; D000118:Acetylglucosaminidase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase